FMO DATABASE

FMODB ID: 1744Z

Calculation Name: 2VW9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2VW9

Chain ID: A

ChEMBL ID:

UniProt ID: O25841

Base Structure: X-ray

Registration Date: 2023-06-21

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	108
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-767500.143564
FMO2-HF: Nuclear repulsion	724644.206361
FMO2-HF: Total energy	-42855.937203
FMO2-MP2: Total energy	-42979.164518

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:1001:MET)

Summations of interaction energy for fragment #1(A:1001:MET)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
0.716	2.946	-0.016	-1.009	-1.205	0.007

Interaction energy analysis for fragmet #1(A:1001:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.036 / q_NPA : 0.014

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	1003	ASN	0	0.012	0.004	3.787	-1.026	1.204	-0.016	-1.009	-1.205	0.007
4	A	1004	LYS	1	0.812	0.897	6.076	1.560	1.560	0.000	0.000	0.000	0.000
5	A	1005	VAL	0	0.011	0.009	9.677	0.140	0.140	0.000	0.000	0.000	0.000
6	A	1006	ILE	0	0.037	0.004	12.922	0.004	0.004	0.000	0.000	0.000	0.000
7	A	1007	MET	0	-0.030	-0.006	16.311	0.030	0.030	0.000	0.000	0.000	0.000
8	A	1008	VAL	0	0.044	0.033	19.307	0.007	0.007	0.000	0.000	0.000	0.000
9	A	1009	GLY	0	0.019	0.023	23.039	0.006	0.006	0.000	0.000	0.000	0.000
10	A	1010	ARG	1	0.863	0.926	25.069	0.183	0.183	0.000	0.000	0.000	0.000
11	A	1011	LEU	0	0.013	0.012	25.897	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	1012	THR	0	-0.032	-0.016	27.412	0.014	0.014	0.000	0.000	0.000	0.000
13	A	1013	ARG	1	0.741	0.818	24.909	0.173	0.173	0.000	0.000	0.000	0.000
14	A	1014	ASN	0	0.034	0.014	30.063	-0.016	-0.016	0.000	0.000	0.000	0.000
15	A	1015	VAL	0	0.006	0.019	26.694	0.000	0.000	0.000	0.000	0.000	0.000
16	A	1016	GLU	-1	-0.799	-0.859	26.736	-0.134	-0.134	0.000	0.000	0.000	0.000
17	A	1017	LEU	0	-0.037	-0.014	26.958	-0.011	-0.011	0.000	0.000	0.000	0.000
18	A	1018	LYS	1	0.918	0.964	25.575	0.116	0.116	0.000	0.000	0.000	0.000
19	A	1019	TYR	0	0.027	-0.008	27.302	-0.010	-0.010	0.000	0.000	0.000	0.000
20	A	1020	LEU	0	-0.036	-0.027	21.857	0.011	0.011	0.000	0.000	0.000	0.000
21	A	1021	PRO	0	0.026	0.004	26.189	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	1022	SER	0	0.008	0.002	23.448	0.002	0.002	0.000	0.000	0.000	0.000
23	A	1023	GLY	0	0.055	0.032	26.576	0.001	0.001	0.000	0.000	0.000	0.000
24	A	1024	SER	0	-0.063	-0.027	22.591	-0.015	-0.015	0.000	0.000	0.000	0.000
25	A	1025	ALA	0	0.040	0.036	24.715	0.010	0.010	0.000	0.000	0.000	0.000
26	A	1026	ALA	0	-0.027	-0.024	22.528	-0.021	-0.021	0.000	0.000	0.000	0.000
27	A	1027	ALA	0	0.025	0.017	22.511	0.019	0.019	0.000	0.000	0.000	0.000
28	A	1028	THR	0	-0.058	-0.011	21.767	-0.024	-0.024	0.000	0.000	0.000	0.000
29	A	1029	ILE	0	0.021	0.026	22.140	0.020	0.020	0.000	0.000	0.000	0.000
30	A	1030	GLY	0	0.056	0.025	22.962	-0.013	-0.013	0.000	0.000	0.000	0.000
31	A	1031	LEU	0	-0.030	-0.007	21.245	0.004	0.004	0.000	0.000	0.000	0.000
32	A	1032	ALA	0	0.022	0.008	24.255	0.011	0.011	0.000	0.000	0.000	0.000
33	A	1033	THR	0	-0.015	-0.030	21.884	-0.006	-0.006	0.000	0.000	0.000	0.000
34	A	1034	SER	0	-0.036	-0.007	24.623	0.003	0.003	0.000	0.000	0.000	0.000
35	A	1035	ARG	1	0.857	0.921	22.658	0.212	0.212	0.000	0.000	0.000	0.000
36	A	1036	ARG	1	0.925	0.947	26.286	0.178	0.178	0.000	0.000	0.000	0.000
37	A	1037	PHE	0	-0.002	0.000	27.170	-0.011	-0.011	0.000	0.000	0.000	0.000
38	A	1038	LYS	1	0.910	0.959	29.239	0.112	0.112	0.000	0.000	0.000	0.000
39	A	1039	LYS	1	0.929	0.962	30.906	0.100	0.100	0.000	0.000	0.000	0.000
40	A	1040	GLN	0	0.007	0.002	32.517	0.000	0.000	0.000	0.000	0.000	0.000
41	A	1041	ASP	-1	-0.623	-0.799	33.868	-0.083	-0.083	0.000	0.000	0.000	0.000
42	A	1042	GLY	0	-0.086	-0.063	37.038	0.000	0.000	0.000	0.000	0.000	0.000
43	A	1043	THR	0	-0.101	-0.048	36.241	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	1044	LEU	0	0.022	0.030	32.650	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	1045	GLY	0	-0.097	-0.066	31.773	0.008	0.008	0.000	0.000	0.000	0.000
46	A	1046	GLU	-1	-0.891	-0.957	29.271	-0.151	-0.151	0.000	0.000	0.000	0.000
47	A	1047	GLU	-1	-0.834	-0.868	23.536	-0.191	-0.191	0.000	0.000	0.000	0.000
48	A	1048	VAL	0	0.007	-0.017	26.302	-0.013	-0.013	0.000	0.000	0.000	0.000
49	A	1049	CYS	0	-0.010	0.001	20.552	0.003	0.003	0.000	0.000	0.000	0.000
50	A	1050	PHE	0	-0.004	-0.006	23.261	-0.008	-0.008	0.000	0.000	0.000	0.000
51	A	1051	ILE	0	0.022	0.004	16.464	0.001	0.001	0.000	0.000	0.000	0.000
52	A	1052	ASP	-1	-0.737	-0.845	20.218	-0.172	-0.172	0.000	0.000	0.000	0.000
53	A	1053	ALA	0	-0.009	-0.008	18.132	-0.031	-0.031	0.000	0.000	0.000	0.000
54	A	1054	ARG	1	0.765	0.836	16.940	0.227	0.227	0.000	0.000	0.000	0.000
55	A	1055	LEU	0	0.024	0.012	17.731	-0.061	-0.061	0.000	0.000	0.000	0.000
56	A	1056	PHE	0	0.034	-0.007	16.374	0.041	0.041	0.000	0.000	0.000	0.000
57	A	1057	GLY	0	0.030	0.023	20.091	-0.022	-0.022	0.000	0.000	0.000	0.000
58	A	1058	ARG	1	0.938	0.932	22.268	0.201	0.201	0.000	0.000	0.000	0.000
59	A	1059	THR	0	0.048	0.027	19.242	0.024	0.024	0.000	0.000	0.000	0.000
60	A	1060	ALA	0	-0.013	0.000	22.254	0.008	0.008	0.000	0.000	0.000	0.000
61	A	1061	GLU	-1	-0.790	-0.881	23.811	-0.153	-0.153	0.000	0.000	0.000	0.000
62	A	1062	ILE	0	-0.040	-0.015	24.520	0.012	0.012	0.000	0.000	0.000	0.000
63	A	1063	ALA	0	0.028	0.001	24.476	0.008	0.008	0.000	0.000	0.000	0.000
64	A	1064	ASN	0	-0.015	-0.026	26.557	0.012	0.012	0.000	0.000	0.000	0.000
65	A	1065	GLN	0	-0.036	0.001	29.413	0.005	0.005	0.000	0.000	0.000	0.000
66	A	1066	TYR	0	-0.048	-0.034	29.394	0.011	0.011	0.000	0.000	0.000	0.000
67	A	1067	LEU	0	-0.032	0.007	26.025	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	1068	SER	0	0.014	0.010	30.404	0.012	0.012	0.000	0.000	0.000	0.000
69	A	1069	LYS	1	0.978	0.977	31.578	0.112	0.112	0.000	0.000	0.000	0.000
70	A	1070	GLY	0	-0.045	-0.014	31.523	0.006	0.006	0.000	0.000	0.000	0.000
71	A	1071	SER	0	0.012	-0.016	30.082	0.001	0.001	0.000	0.000	0.000	0.000
72	A	1072	SER	0	-0.057	-0.028	28.400	-0.007	-0.007	0.000	0.000	0.000	0.000
73	A	1073	VAL	0	-0.057	-0.036	23.884	0.003	0.003	0.000	0.000	0.000	0.000
74	A	1074	LEU	0	0.026	0.011	19.868	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	1075	ILE	0	-0.012	0.000	16.771	0.000	0.000	0.000	0.000	0.000	0.000
76	A	1076	GLU	-1	-0.795	-0.881	14.316	-0.888	-0.888	0.000	0.000	0.000	0.000
77	A	1077	GLY	0	-0.008	-0.001	13.145	0.055	0.055	0.000	0.000	0.000	0.000
78	A	1078	ARG	1	0.890	0.951	8.397	0.900	0.900	0.000	0.000	0.000	0.000
79	A	1079	LEU	0	0.015	-0.006	9.174	0.245	0.245	0.000	0.000	0.000	0.000
80	A	1080	THR	0	-0.041	-0.034	9.093	-0.133	-0.133	0.000	0.000	0.000	0.000
81	A	1081	TYR	0	0.030	0.014	11.038	0.068	0.068	0.000	0.000	0.000	0.000
82	A	1082	GLU	-1	-0.784	-0.851	12.578	-0.118	-0.118	0.000	0.000	0.000	0.000
83	A	1083	SER	0	0.025	0.006	15.765	0.021	0.021	0.000	0.000	0.000	0.000
84	A	1084	TRP	0	-0.034	-0.015	17.620	0.004	0.004	0.000	0.000	0.000	0.000
85	A	1085	MET	0	0.057	0.055	21.073	0.004	0.004	0.000	0.000	0.000	0.000
86	A	1086	ASP	-1	-0.769	-0.878	24.746	0.023	0.023	0.000	0.000	0.000	0.000
87	A	1087	GLN	0	0.029	-0.008	27.213	0.006	0.006	0.000	0.000	0.000	0.000
88	A	1088	THR	0	-0.029	0.007	30.326	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	1089	GLY	0	0.004	0.009	29.248	0.005	0.005	0.000	0.000	0.000	0.000
90	A	1090	LYS	1	0.839	0.903	27.085	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	1091	LYS	1	0.888	0.917	22.495	-0.125	-0.125	0.000	0.000	0.000	0.000
92	A	1092	ASN	0	-0.027	-0.006	22.515	-0.013	-0.013	0.000	0.000	0.000	0.000
93	A	1093	SER	0	-0.008	-0.005	17.290	0.024	0.024	0.000	0.000	0.000	0.000
94	A	1094	ARG	1	0.830	0.893	17.244	0.116	0.116	0.000	0.000	0.000	0.000
95	A	1095	HIS	0	0.049	0.047	12.594	-0.030	-0.030	0.000	0.000	0.000	0.000
96	A	1096	THR	0	-0.086	-0.058	14.585	-0.011	-0.011	0.000	0.000	0.000	0.000
97	A	1097	ILE	0	0.070	0.036	13.814	-0.054	-0.054	0.000	0.000	0.000	0.000
98	A	1098	THR	0	-0.048	0.009	12.574	0.089	0.089	0.000	0.000	0.000	0.000
99	A	1099	ALA	0	0.005	-0.007	13.628	-0.129	-0.129	0.000	0.000	0.000	0.000
100	A	1100	ASP	-1	-0.859	-0.928	12.276	-1.021	-1.021	0.000	0.000	0.000	0.000
101	A	1101	SER	0	-0.060	-0.029	15.692	0.082	0.082	0.000	0.000	0.000	0.000
102	A	1102	LEU	0	0.024	-0.005	18.927	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	1103	GLN	0	0.013	0.012	22.002	0.031	0.031	0.000	0.000	0.000	0.000
104	A	1104	PHE	0	0.011	0.002	24.353	0.005	0.005	0.000	0.000	0.000	0.000
105	A	1105	MET	0	0.006	0.004	26.641	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	1106	ASP	-1	-0.720	-0.823	29.695	-0.178	-0.178	0.000	0.000	0.000	0.000
107	A	1107	LYS	1	0.951	0.989	33.024	0.169	0.169	0.000	0.000	0.000	0.000
108	A	1108	LYS	1	0.874	0.929	32.250	0.182	0.182	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1001:MET)